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Extracellular catalase activity protects cysteine cathepsins from inactivation by hydrogen peroxide
Author(s) -
Hervé-Grépinet Virginie,
Veillard Florian,
Godat Emmanuel,
Heuzé-Vourc'h Nathalie,
Lecaille Fabien,
Lalmanach Gilles
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.03.007
Subject(s) - cathepsin , catalase , extracellular , proteases , biochemistry , cysteine , chemistry , cathepsin b , hydrogen peroxide , cathepsin h , cathepsin l , cathepsin s , cysteine protease , cathepsin o , microbiology and biotechnology , enzyme , biology
The resistance of secreted cysteine cathepsins to peroxide inactivation was evaluated using as model THP‐1 cells. Differentiated cells released mostly cathepsin B, but also cathepsins H, K, and L, with a maximum of endopeptidase activity at day 6. Addition of non‐cytotoxic concentrations of H 2 O 2 did not affect mRNA expression levels and activity of cathepsins, while the catalase activity remained also unchanged, consistently with RT‐PCR analysis. Conversely inhibition of extracellular catalase led to a striking inactivation of secreted cysteine cathepsins by H 2 O 2 . This report suggests that catalase may participate in the protection of extracellular cysteine proteases against peroxidation.